ID A0A1X9TV11_9LACO Unreviewed; 487 AA. AC A0A1X9TV11; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 28-JUN-2023, entry version 20. DE RecName: Full=Cardiolipin synthase {ECO:0000256|HAMAP-Rule:MF_01916}; DE Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_01916}; DE EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_01916}; GN ORFNames=LDE01_01390 {ECO:0000313|EMBL:BBL26842.1}; OS Lactobacillus delbrueckii subsp. delbrueckii. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=83684 {ECO:0000313|EMBL:BBL26842.1, ECO:0000313|Proteomes:UP000319966}; RN [1] {ECO:0000313|EMBL:BBL26842.1, ECO:0000313|Proteomes:UP000319966} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 3202 {ECO:0000313|EMBL:BBL26842.1, RC ECO:0000313|Proteomes:UP000319966}; RA Miura T., Furukawa M., Shimamura M., Ohyama Y., Yamazoe A., Kawasaki H.; RT "Complete genome sequence of Lactobacillus delbrueckii subsp. delbrueckii RT NBRC 3202."; RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one CC phosphatidylglycerol molecule to another to form cardiolipin (CL) CC (diphosphatidylglycerol) and glycerol. {ECO:0000256|HAMAP- CC Rule:MF_01916}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a CC cardiolipin + glycerol; Xref=Rhea:RHEA:31451, ChEBI:CHEBI:17754, CC ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01916}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01916}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01916}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01916}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP019750; BBL26842.1; -; Genomic_DNA. DR RefSeq; WP_072546917.1; NZ_CP021136.1. DR EnsemblBacteria; ARR37751; ARR37751; B9N98_06265. DR Proteomes; UP000319966; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008808; F:cardiolipin synthase activity; IEA:InterPro. DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro. DR CDD; cd09110; PLDc_CLS_1; 1. DR CDD; cd09112; PLDc_CLS_2; 1. DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2. DR HAMAP; MF_01916; Cardiolipin_synth_Cls; 1. DR InterPro; IPR030874; Cardiolipin_synth_Firmi. DR InterPro; IPR022924; Cardiolipin_synthase. DR InterPro; IPR027379; CLS_N. DR InterPro; IPR025202; PLD-like_dom. DR InterPro; IPR001736; PLipase_D/transphosphatidylase. DR PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1. DR PANTHER; PTHR21248:SF22; PHOSPHOLIPASE D; 1. DR Pfam; PF13091; PLDc_2; 2. DR Pfam; PF13396; PLDc_N; 1. DR SMART; SM00155; PLDc; 2. DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2. DR TIGRFAMs; TIGR04265; bac_cardiolipin; 1. DR PROSITE; PS50035; PLD; 2. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_01916}; KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP- KW Rule:MF_01916}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP- KW Rule:MF_01916}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01916}; KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209, KW ECO:0000256|HAMAP-Rule:MF_01916}; KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP- KW Rule:MF_01916}; Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01916}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01916}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01916}. FT TRANSMEM 6..26 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" FT TRANSMEM 33..56 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" FT ACT_SITE 221 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" FT ACT_SITE 223 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" FT ACT_SITE 228 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" FT ACT_SITE 405 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" FT ACT_SITE 407 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" FT ACT_SITE 412 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916" SQ SEQUENCE 487 AA; 56307 MW; A2469E1069571E09 CRC64; MTAISWIDIW HIIFFANAIL ALWTVFHRKR SVAASWAWLI VLIILPVVGF IIYVFVGRGI SQENLFAINR QKHIGLSNVQ KMITEAPAKI DQNDTSPSAH ILIKYLDKDQ ESPITKNNKL KLYTDGHDKF RDLFADIRQA KSSINVEYYT IYNDAIGNEF LKLLIQKAKE GVQVRVLYDA WGSFGASKSW FNQLTEAGGD VLPFITSRNM ISRNRINYHL HRKIVVIDGV TSWTGGFNVG DQYLGRKKKF GYWRDTHLRL VGSASLLLQE RFVMDWNASA VKEEELISFD EKLFPDLDEN DISKGDMAVQ VVSDGPDNDE PYMRNGLVRL MMLARKRVWI QTPYLIPDEA MIAAWQILAS SGVDLRIMIP CMPDHPFIYR ATQWYANQLV KIGVKVYTYN NGFMHAKTII VDDKYATVGS VNQDYRSYDL NFEDNVFVYD RAFNKEMSDQ FEKDMEQSTL LTPEMIKKQS RWLRFLQNFS RLLSPIL //